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Michael T. White, S. Nandi, Biochemical Studies on Mitochondria Isolated From Normal and Neoplastic Tissues of the Mouse Mammary Gland, JNCI: Journal of the National Cancer Institute, Volume 56, Issue 1, January 1976, Pages 65–73, https://doi.org/10.1093/jnci/56.1.65
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Summary
Mitochondria isolated from spontaneous and transplanted mammary adenocarcinomas of two strains of mice were compared, by various biochemical criteria, to mitochondria from mammary glands of midpregnant or hormonally stimulated, cancer-free mice. The specific activities of several mitochondrial enzymes including cytochrome oxidase, α-glycerophosphate oxidase, and succinate dehydrogenase were twofold to threefold lower, whereas the activity of monoamine oxidase was twofold higher in tumor mitochondria. Malate dehydrogenase, adenylate kinase, and NADH oxidase showed similar levels of activity in tumor and midpregnant mammary gland mitochondria. In addition, mitochondrial polypeptide composition was analyzed by electrophoresis on sodium dodecyl sulfate-urea polyacrylamide gels. Midpregnant mammary gland and mammary tumor mitochondria were similar in polypeptide composition; however, several differences were observed. A high-molecular-weight polypeptide, present in midpregnant mammary gland mitochondria was absent from tumor mitochondria. Also, tumor mitochondria contained an additional high-molecular-weight polypeptide not found in the midpregnant mammary gland. There were numerous differences in the relative proportions of many polypeptides common to both tumor and midpregnant mammary gland mitochondria.
- mitochondria
- cancer
- adenocarcinoma
- adenylate kinase
- cytochrome c oxidase
- electrophoresis
- gel
- glycerophosphates
- animal mammary neoplasms
- monoamine oxidase
- nicotinamide adenine dinucleotide (nad)
- peptides
- succinate dehydrogenase
- breast
- enzymes
- malate dehydrogenase
- mice
- neoplasms
- sodium
- urea
- sulfate
- oxidase